1IF2

X-RAY STRUCTURE OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH IPP

1IF2 の概要

• エントリーDOI: 10.2210/pdb1if2/pdb
• 分子名称: TRIOSEPHOSPHATE ISOMERASE, [2(FORMYL-HYDROXY-AMINO)-ETHYL]-PHOSPHONIC ACID (3 entities in total)
• 機能のキーワード: tim barrel, transition state analogue, isomerase
• 由来する生物種: Leishmania mexicana
• 細胞内の位置: Cytoplasm: P48499
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27377.31

構造登録者

Kursula, I.,Partanen, S.,Lambeir, A.-M.,Antonov, D.M.,Augustyns, K.,Wierenga, R.K. (登録日: 2001-04-12, 公開日: 2001-08-17, 最終更新日: 2024-02-07)

主引用文献

Kursula, I.,Partanen, S.,Lambeir, A.M.,Antonov, D.M.,Augustyns, K.,Wierenga, R.K.
Structural determinants for ligand binding and catalysis of triosephosphate isomerase.
Eur.J.Biochem., 268:5189-5196, 2001

PubMed Abstract: The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate D-glyceraldehyde-3-phosphate, and it is observed to bind with its aldehyde oxygen in an oxyanion hole formed by ND2 of Asn11 and NE2 of His95. Comparison of the mode of binding of IPP and the transition state analogue phosphoglycolohydroxamate (PGH) suggests that the Glu167 side chain, as well as the triose part of the substrate, adopt different conformations as the catalysed reaction proceeds. Comparison of the TIM-IPP and the TIM-PGH structures with other liganded and unliganded structures also highlights the conformational flexibility of the ligand and the active site, as well as the conserved mode of ligand binding.

PubMed: 11589711
DOI: 10.1046/j.0014-2956.2001.02452.x

実験手法

X-RAY DIFFRACTION (2 Å)